A lipase with broad solvent stability from Burkholderia cepacia RQ3: isolation, characteristics and application for chiral resolution of 1-phenylethanol

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• 作者：Chengjia Xie ; Bin Wu ; Song Qin ; Bingfang He
• 关键词：Burkholderia cepacia ; 1 ; phenylethanol ; Organic solvent ; stable ; Lipase
• 刊名：Bioprocess and Biosystems Engineering
• 出版年：2016
• 出版时间：January 2016
• 年：2016
• 卷：39
• 期：1
• 页码：59-66
• 全文大小：899 KB
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• 作者单位：Chengjia Xie (1)
  Bin Wu (2)
  Song Qin (3)
  Bingfang He (3)
  
  1. School of Chemical Engineering, Yangzhou Polytechnic Institute, 199 Huayang West Road, Yangzhou, 225127, Jiangsu, China
  2. College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, 30 Puzhunan Road, Nanjing, 211816, Jiangsu, China
  3. School of Pharmaceutical Sciences, Nanjing Tech University, 30 Puzhunan Road, Nanjing, 211816, Jiangsu, China
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Biotechnology
  Industrial Chemistry and Chemical Engineering
  Industrial and Production Engineering
  Waste Management and Waste Technology
  Waste Water Technology, Water Pollution Control, Water Management and Aquatic Pollution
  Food Science
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：1615-7605

文摘

Using both polar and low polar organic solvents (DMSO and toluene) as screening stress, a solvent-stable bacterium Burkholderia cepacia RQ3 was newly isolated. An organic solvent-stable lipase from strain RQ3 was purified in a single step with 50.1 % recovery by hydrophobic chromatography. The purified lipase was homogenous on SDS-PAGE and had an apparent molecular mass of 33 kDa. The gene of lipase RQ3 with an open reading frame of 1095 bp encoding 364-amino acid residues was cloned. The optimal pH and temperature for lipase activity were 9.0 and 40 °C. The lipase was stable in a wide pH range of 6.0–10.0 and at temperature below 50 °C. Strikingly, all the tested hydrophilic and hydrophobic organic solvents significantly extended the half-life of lipase RQ3 compared with that in a solvent-free system, which indicated that lipase RQ3 showed a broad solvent tolerance to various organic solvents. The lipase demonstrated excellent enantioselective transesterification toward the (S)-1-phenylethanol with a theoretical conversion yield of 50 % and ee _p of 99.9 %, which made it an exploitable biocatalyst for organic synthesis and pharmaceutical industries.